Identification of molecular interactions between P-site tRNA and the ribosome essential for translocation
Identification of molecular interactions between P-site tRNA and the ribosome essential for translocation
复制标题
DOI:
10.1073/pnas.211184098
复制
发表时间:
2001-09-25
影响因子:
11.1
通讯作者:
Joseph, S
中科院分区:
文献类型:
--
作者:
Feinberg, JS;Joseph, S
Translocation of the tRNA-mRNA complex is a fundamental step in the elongation cycle of protein synthesis. Our studies show that the ribosome can translocate a P-site-bound tRNA(Met) with a break in the phosphodiester backbone between positions 56 and 57 in the T psiC-loop. We have used this fragmented P-site-bound tRNAMet to identify two 2 ' -hydroxyl groups at positions 71 and 76 in the 3 ' -acceptor arm that are essential for translocation. Crystallographic data show that the 2 ' -hydroxyl group at positions 71 and 76 contacts the backbone of 235 rRNA residues 1892 and 2433-2434, respectively, in the ribosomal E site. These results establish a set of functional interactions between P-site tRNA and 235 rRNA that are essential for translocation.